DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252991X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252994X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252990X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252996X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252987X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252995X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252997X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252992X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252989X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252998X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252986X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions ecolx Escherichia coli ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252988X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nature structural & molecular biology 2013 imex curation Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Gueneau E., Dherin C., Legrand P., Tellier-Lebegue C., Gilquin B., Bonnesoeur P., Londino F., Quemener C., Le Du MH., Márquez JA., Moutiez M., Gondry M., Boiteux S., Charbonnier JB. DIP original experiment: DIP-252993X Nature structural & molecular biology 2013 IMEx Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. pms1_yeast DNA mismatch repair protein PMS1 PMS1 YNL082W N2317 Postmeiotic segregation protein 1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MTQIHQINDIDVHRITSGQVITDLTTAVKELVDNSIDANANQIEIIFKDYGLESIECSDNGDGIDPSNYEFLALKHYTSKIAKFQDVAKVQTLGFRGEALSSLCGIAKLSVITTTSPPKADKLEYDMVGHITSKTTTSRNKGTTVLVSQLFHNLPVRQKEFSKTFKRQFTKCLTVIQGYAIINAAIKFSVWNITPKGKKNLILSTMRNSSMRKNISSVFGAGGMRGLEEVDLVLDLNPFKNRMLGKYTDDPDFLDLDYKIRVKGYISQNSFGCGRNSKDRQFIYVNKRPVEYSTLLKCCNEVYKTFNNVQFPAVFLNLELPMSLIDVNVTPDKRVILLHNERAVIDIFKTTLSDYYNRQELALPKRMCSQSEQQAQKRLKTEVFDDRSTTHESDNENYHTARSESNQSNHAHFNSTTGVIDKSNGTELTSVMDGNYTNVTDVIGSECEVSVDSSVVLDEGNSSTPTKKLPSIKTDSQNLSDLNLNNFSNPEFQNITSPDKARSLEKVVEEPVYFDIDGEKFQEKAVLSQADGLVFVDNECHEHTNDCCHQERRGSTDTEQDDEADSIYAEIEPVEINVRTPLKNSRKSISKDNYRSLSDGLTHRKFEDEILEYNLSTKNFKEISKNGKQMSSIISKRKSEAQENIIKNKDELEDFEQGEKYLTLTVSKNDFKKMEVVGQFNLGFIIVTRKVDNKYDLFIVDQHASDEKYNFETLQAVTVFKSQKLIIPQPVELSVIDELVVLDNLPVFEKNGFKLKIDEEEEFGSRVKLLSLPTSKQTLFDLGDFNELIHLIKEDGGLRRDNIRCSKIRSMFAMRACRSSIMIGKPLNKKTMTRVVHNLSELDKPWNCPHGRPTMRHLMELRDWSSFSKDYEI 2E0FFBC59B718854 2E0FFBC59B718854 exo1_yeast Exodeoxyribonuclease 1 EXO1 DHS1 YOR033C OR26.23 Exodeoxyribonuclease I Protein DHS1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MGIQGLLPQLKPIQNPVSLRRYEGEVLAIDGYAWLHRAACSCAYELAMGKPTDKYLQFFIKRFSLLKTFKVEPYLVFDGDAIPVKKSTESKRRDKRKENKAIAERLWACGEKKNAMDYFQKCVDITPEMAKCIICYCKLNGIRYIVAPFEADSQMVYLEQKNIVQGIISEDSDLLVFGCRRLITKLNDYGECLEICRDNFIKLPKKFPLGSLTNEEIITMVCLSGCDYTNGIPKVGLITAMKLVRRFNTIERIILSIQREGKLMIPDTYINEYEAAVLAFQFQRVFCPIRKKIVSLNEIPLYLKDTESKRKRLYACIGFVIHRETQKKQIVHFDDDIDHHLHLKIAQGDLNPYDFHQPLANREHKLQLASKSNIEFGKTNTTNSEAKVKPIESFFQKMTKLDHNPKVANNIHSLRQAEDKLTMAIKRRKLSNANVVQETLKDTRSKFFNKPSMTVVENFKEKGDSIQDFKEDTNSQSLEEPVSESQLSTQIPSSFITTNLEDDDNLSEEVSEVVSDIEEDRKNSEGKTIGNEIYNTDDDGDGDTSEDYSETAESRVPTSSTTSFPGSSQRSISGCTKVLQKFRYSSSFSGVNANRQPLFPRHVNQKSRGMVYVNQNRDDDCDDNDGKNQITQRPSLRKSLIGARSQRIVIDMKSVDERKSFNSSPILHEESKKRDIETTKSSQARPAVRSISLLSQFVYKGK 78E22F6B265DB3AA 78E22F6B265DB3AA mlh1_yeast DNA mismatch repair protein MLH1 MLH1 YMR167W YM8520.16 PMS2 MutL protein homolog 1 Post meiotic segregation protein 2 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSLRIKALDASVVNKIAAGEIIISPVNALKEMMENSIDANATMIDILVKEGGIKVLQITDNGSGINKADLPILCERFTTSKLQKFEDLSQIQTYGFRGEALASISHVARVTVTTKVKEDRCAWRVSYAEGKMLESPKPVAGKDGTTILVEDLFFNIPSRLRALRSHNDEYSKILDVVGRYAIHSKDIGFSCKKFGDSNYSLSVKPSYTVQDRIRTVFNKSVASNLITFHISKVEDLNLESVDGKVCNLNFISKKSISPIFFINNRLVTCDLLRRALNSVYSNYLPKGNRPFIYLGIVIDPAAVDVNVHPTKREVRFLSQDEIIEKIANQLHAELSAIDTSRTFKASSISTNKPESLIPFNDTIESDRNRKSLRQAQVVENSYTTANSQLRKAKRQENKLVRIDASQAKITSFLSSSQQFNFEGSSTKRQLSEPKVTNVSHSQEAEKLTLNESEQPRDANTINDNDLKDQPKKKQKLGDYKVPSIADDEKNALPISKDGYIRVPKERVNVNLTSIKKLREKVDDSIHRELTDIFANLNYVGVVDEERRLAAIQHDLKLFLIDYGSVCYELFYQIGLTDFANFGKINLQSTNVSDDIVLYNLLSEFDELNDDASKEKIISKIWDMSSMLNEYYSIELVNDGLDNDLKSVKLKSLPLLLKGYIPSLVKLPFFIYRLGKEVDWEDEQECLDGILREIALLYIPDMVPKVDTSDASLSEDEKAQFINRKEHISSLLEHVLFPCIKRRFLAPRHILKDVVEIANLPDLYKVFERC B2DBB31DE3943171 B2DBB31DE3943171 sgs1_yeast ATP-dependent helicase SGS1 SGS1 TPS1 YMR190C YM9646.02C Helicase TPS1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MVTKPSHNLRREHKWLKETATLQEDKDFVFQAIQKHIANKRPKTNSPPTTPSKDECGPGTTNFITSIPASGPTNTATKQHEVMQTLSNDTEWLSYTATSNQYADVPMVDIPASTSVVSNPRTPNGSKTHNFNTFRPHMASSLVENDSSRNLGSRNNNKSVIDNSSIGKQLENDIKLEVIRLQGSLIMALKEQSKLLLQKCSIIESTSLSEDAKRLQLSRDIRPQLSNMSIRIDSLEKEIIKAKKDGMSKDQSKGRSQVSSQDDNIISSILPSPLEYNTSSRNSNLTSTTATTVTKALAITGAKQNITNNTGKNSNNDSNNDDLIQVLDDEDDIDCDPPVILKEGAPHSPAFPHLHMTSEEQDELTRRRNMRSREPVNYRIPDRDDPFDYVMGKSLRDDYPDVEREEDELTMEAEDDAHSSYMTTRDEEKEENELLNQSDFDFVVNDDLDPTQDTDYHDNMDVSANIQESSQEGDTRSTITLSQNKNVQVILSSPTAQSVPSNGQNQIGVEHIDLLEDDLEKDAILDDSMSFSFGRQHMPMSHSDLELIDSEKENEDFEEDNNNNGIEYLSDSDLERFDEERENRTQVADIQELDNDLKIITERKLTGDNEHPPPSWSPKIKREKSSVSQKDEEDDFDDDFSLSDIVSKSNLSSKTNGPTYPWSDEVLYRLHEVFKLPGFRPNQLEAVNATLQGKDVFVLMPTGGGKSLCYQLPAVVKSGKTHGTTIVISPLISLMQDQVEHLLNKNIKASMFSSRGTAEQRRQTFNLFINGLLDLVYISPEMISASEQCKRAISRLYADGKLARIVVDEAHCVSNWGHDFRPDYKELKFFKREYPDIPMIALTATASEQVRMDIIHNLELKEPVFLKQSFNRTNLYYEVNKKTKNTIFEICDAVKSRFKNQTGIIYCHSKKSCEQTSAQMQRNGIKCAYYHAGMEPDERLSVQKAWQADEIQVICATVAFGMGIDKPDVRFVYHFTVPRTLEGYYQETGRAGRDGNYSYCITYFSFRDIRTMQTMIQKDKNLDRENKEKHLNKLQQVMAYCDNVTDCRRKLVLSYFNEDFDSKLCHKNCDNCRNSANVINEERDVTEPAKKIVKLVESIQNERVTIIYCQDVFKGSRSSKIVQANHDTLEEHGIGKSMQKSEIERIFFHLITIRVLQEYSIMNNSGFASSYVKVGPNAKKLLTGKMEIKMQFTISAPNSRPSTSSSFQANEDNIPVIAQKSTTIGGNVAANPPRFISAKEHLRSYTYGGSTMGSSHPITLKNTSDLRSTQELNNLRMTYERLRELSLNLGNRMVPPVGNFMPDSILKKMAAILPMNDSAFATLGTVEDKYRRRFKYFKATIADLSKKRSSEDHEKYDTILNDEFVNRAAASSNGIAQSTGTKSKFFGANLNEAKENEQIINQIRQSQLPKNTTSSKSGTRSISKSSKKSANGRRGFRNYRGHYRGRK 0DC320B41756A3C3 0DC320B41756A3C3 mlh3_yeast DNA mismatch repair protein MLH3 MLH3 MutL protein homolog 3 P2550 YPL164C protein protein yeast Saccharomyces cerevisiae Baker's yeast MSQHIRKLDSDVSERLKSQACTVSLASAVREIVQNSVDAHATTIDVMIDLPNLSFAVYDDGIGLTRSDLNILATQNYTSKIRKMNDLVTMKTYGYRGDALYSISNVSNLFVCSKKKDYNSAWMRKFPSKSVMLSENTILPIDPFWKICPWSRTKSGTVVIVEDMLYNLPVRRRILKEEPPFKTFNTIKADMLQILVMHPMISLNVQYTDKLRINTEVLFRSKNITEGLTKHQQMSQVLRNVFGAIIPPDMLKKVSLKFNEYQIEGIISKMPVGLKDLQFIYINGRRYADSAFQGYVDSLFQAQDFGEKGMSLLKTKSVGKPYRSHPVFILDVRCPQTIDDLLQDPAKKIVKPSHIRTIEPLIVKTIRSFLTFQGYLTPDKSDSSFEIVNCSQKTATLPDSRIQISKRNQVLNSKMKIARINSYIGKPAVNGCRINNSTINYEKIKNIRIDGQKSRLRNKLSSRPYDSGFTEDYDSIGKTITDFSISRSVLAKYEVINQVDKKFILIRCLDQSIHNCPLLVLVDQHACDERIRLEELFYSLLTEVVTGTFVARDLKDCCIEVDRTEADLFKHYQSEFKKWGIGYETIEGTMETSLLEIKTLPEMLTSKYNGDKDYLKMVLLQHAHDLKDFKKLPMDLSHFENYTSVDKLYWWKYSSCVPTVFHEILNSKACRSAVMFGDELTRQECIILISKLSRCHNPFECAHGRPSMVPIAELK 970FD7F57EB6E3B1 970FD7F57EB6E3B1 nth2_yeast Endonuclease III homolog 2 NTG2 Endonuclease III-like glycosylase 2 Redoxyendonuclease 2 SCR2 YOL043C Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 2 protein protein yeast Saccharomyces cerevisiae Baker's yeast MREESRSRKRKHIPVDIEEVEVRSKYFKKNERTVELVKENKINKDLQNYGGVNIDWIKALKPIEYFEWIESRTCDDPRTWGRPITKEEMINDSGAKVPESFLPIYNRVRLMRSKVKTPVDAMGCSMIPVLVSNKCGIPSEKVDPKNFRLQFLIGTMLSAQTRDERMAQAALNITEYCLNTLKIAEGITLDGLLKIDEPVLANLIRCVSFYTRKANFIKRTAQLLVDNFDSDIPYDIEGILSLPGVGPKMGYLTLQKGWGLIAGICVDVHVHRLCKMWNWVDPIKCKTAEHTRKELQVWLPHSLWYEINTVLVGFGQLICMARGKRCDLCLANDVCNARNEKLIESSKFHQLEDKEDIEKVYSHWLDTVTNGITTERHKKK 517F81C3BA3DDCF7 517F81C3BA3DDCF7 ntg2-mlh1-1 13 19 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 16 unspecified role unspecified role prey prey C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P38920:p.Leu511Ala L511A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain L A This feature has been corrected as a result of our quality control procedures. The original label was 'L511A'. Wed May 02 20:30:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu511ala' Tue Jun 30 19:53:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu511Ala' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association mlh1-pms1-4 11 14 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 635-873 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mlh1-sgs1-1 7 17 unspecified role unspecified role unspecified role unspecified role region 1381-1388 region 1381-1388 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction exo1-mlh1-1 3 15 unspecified role unspecified role unspecified role unspecified role Region 443-450 Region 443-450 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 635-873 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association exo1-mlh1-2 2 15 unspecified role unspecified role bait bait C-terminal domain Region 400-702 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 16 unspecified role unspecified role prey prey C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P38920:p.Leu511Ala L511A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain L A This feature has been corrected as a result of our quality control procedures. The original label was 'L511A'. Wed May 02 15:53:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu511ala' Tue Jun 30 18:11:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu511Ala' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association pms1-mlh1-2 5 14 unspecified role unspecified role bait bait C-terminal domain Region 635-873 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain MBP-tag MBP-tag mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 16 unspecified role unspecified role prey prey C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association mlh1-ntg2-1 10 19 unspecified role unspecified role unspecified role unspecified role Region 22-29 Region 22-29 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q08214:p.Tyr26Phe Y26F mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Y F This feature has been corrected as a result of our quality control procedures. The original label was 'Y26F'. Wed May 02 18:59:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr26phe' Tue Jun 30 17:42:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr26Phe' Q08214:p.Phe27Ala F27A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F27A'. Wed May 02 18:29:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe27ala' Tue Jun 30 19:56:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe27Ala' Q08214:p.Phe27Tyr F27Y mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F Y This feature has been corrected as a result of our quality control procedures. The original label was 'F27Y'. Wed May 02 19:02:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe27tyr' Tue Jun 30 17:53:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe27Tyr' in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mlh3-mlh1-1 6 18 unspecified role unspecified role bait bait C-terminal domain Region 460-715 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 16 unspecified role unspecified role prey prey C-terminal domain Region485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association mlh1-pms1-5 12 14 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 635-873 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pms1-mlh1-3 1 14 unspecified role unspecified role bait bait C-terminal domain Region 611-873 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P14242:p.Asp870Ala D870A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D870A'. Wed May 02 19:46:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp870ala' Tue Jun 30 18:38:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp870Ala' Region 864-873 Region 864-873 required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 16 unspecified role unspecified role prey prey C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association pms1-mlh1-4 8 14 unspecified role unspecified role bait bait C-terminal domain Region 611-873 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 16 unspecified role unspecified role prey prey C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P38920:p.Arg547Ala R547A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R547A'. Wed May 02 18:34:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg547ala' Tue Jun 30 17:10:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg547Ala' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association exo1-mlh1-3 4 15 unspecified role unspecified role unspecified role unspecified role Region 443-450 Region 443-450 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mlh1-ntg2-2 9 19 unspecified role unspecified role unspecified role unspecified role Region 22-29 Region 22-29 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 635-873 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 485-769 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association